Journal
COORDINATION CHEMISTRY REVIEWS
Volume 256, Issue 19-20, Pages 2202-2218Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.ccr.2012.03.038
Keywords
Copper; Octarepeats; Hexarepeats; PrP amyloidogenic region; Doppel; Stability constants; Binding modes of Cu2+ ion; Protective or toxic PrP effects
Categories
Funding
- MIUR [PRIN 2008F5A3AF_005, FIRB RBPR05JH2P, FIRB RBNE08HWLZ]
- University of Catania (Progetto di Ateneo)
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The review describes the stability and the coordination modes of Cu2+ complexes with different regions of N-terminus prion proteins. The structural features of the different metal species are correlated both with the Cu2+-driven redox properties and with the conformational changes induced by the Cu2+ in the different metal binding regions of the protein. The formation of mixed metal complexes is also discussed. We emphasize that binding features should be discussed by referring to the species that actually forms under specific conditions (pH, buffer, etc.) rather than to the binding site; correlating properties with the structures of the so called 'binding sites' may lead to misinterpretation of the experimental results, since a 'binding site' often corresponds to a mixture of species. We also highlight that ignoring species that form with ligands other than the prion peptide (e.g. the buffer) may lead to underestimating their role in crucial processes (e.g. redox activity). (C) 2012 Elsevier B.V. All rights reserved.
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